Dye-linked D-amino acid dehydrogenases: biochemical characteristics and applications in biotechnology.
Appl Microbiol Biotechnol
; 99(22): 9337-47, 2015 Nov.
Article
en En
| MEDLINE
| ID: mdl-26362681
ABSTRACT
Dye-linked D-amino acid dehydrogenases (Dye-DADHs) catalyze the dehydrogenation of free D-amino acids in the presence of an artificial electron acceptor. Although Dye-DADHs functioning in catabolism of L-alanine and as primary enzymes in electron transport chains are widely distributed in mesophilic Gram-negative bacteria, biochemical and biotechnological information on these enzymes remains scanty. This is in large part due to their instability after isolation. On the other hand, in the last decade, several novel types of Dye-DADH have been found in thermophilic bacteria and hyperthermophilic archaea, where they contribute not only to L-alanine catabolism but also to the catabolism of other amino acids, including D-arginine and L-hydroxyproline. In this minireview, we summarize recent developments in our understanding of the biochemical characteristics of Dye-DADHs and their specific application to electrochemical biosensors.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Biotecnología
/
Archaea
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D-Aminoácido Oxidasa
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Aminoácidos
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Bacterias Gramnegativas
Idioma:
En
Revista:
Appl Microbiol Biotechnol
Año:
2015
Tipo del documento:
Article
País de afiliación:
Japón